Viswanathan Raghuram

TL;DR: The results support a molecular model in which bivalent NHERF PDZ domains regulate channel gating by crosslinking the C-terminal tails in a single dimeric CFTR channel, and the magnitude of this regulation is coupled to the stoichiometry of these interactions.

TL;DR: Regulation of CFTR by AMPK may be important in inhibiting CFTR under conditions of metabolic stress, thereby linking transepithelial transport to cell metabolic state.

TL;DR: The results identify a role for PKC and suggest that phosphorylation of NHERF PDZ2 domain may be an important mechanism for regulating CFTR channel activity.

TL;DR: Coexpression of NHERF-2 with ROMK and CFTR dramatically increases the amount ofROMK protein that coimmunopurifies and functionally interacts with CFTR, raising the possibility that PDZ-based interactions may underscore physiological regulation and membrane targeting of ROMK in the kidney.

TL;DR: The results suggest that if cellular expression of multiple InsP3R isoforms is a mechanism to modify the temporal and spatial features of [Ca2+]i signals, then it must be achieved by isoform-specific regulation or localization of various types ofInsP3Rs that have relatively similar Ca2+ permeation properties.